ArticleCommunications biology2022
Docking-guided rational engineering of a macrolide glycosyltransferase glycodiversifies epothilone B.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Functional analysis of a UDP-glucosyltransferase gene contributing to biosynthesis of the flavonol triglycoside in tea plants.Horticulture research · 2025Article
- Anchor Peptide-Based Immobilization Strategy Promote the Applications of Pickering Emulsion System in Natural Products Glycosylation.Angewandte Chemie (International ed. in English) · 2025Article
- Mining versatile feruloyl esterases: phylogenetic classification, structural features, and deep learning model.Bioresources and bioprocessing · 2025Article
- Improving the Catalytic Properties of Xylanase from Alteromones Macleadii H35 Through Sequence Analysis.Applied biochemistry and biotechnology · 2024Article
- Review
- A novel HER2 targeting nanoagent self-assembled from affibody-epothilone B conjugate for cancer therapy.Journal of nanobiotechnology · 2024Article
- Unnatural activities and mechanistic insights of cytochrome P450 PikC gained from site-specific mutagenesis by non-canonical amino acids.Nature communications · 2023Article
- Crystal structure of the lipopolysaccharide outer core galactosyltransferase WaaB involved in pathogenic bacterial invasion of host cells.Frontiers in microbiology · 2023Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosyltransferases typically display acceptor substrate flexibility but more stringent donor specificity. BsGT-1 is a highly effective glycosyltransferase to glycosylate macrolides, including epothilones, promising antitumor compounds. Here, we show that BsGT-1 has three major regions significantly influencing the glycodiversification of epothilone B based on structural molecular docking, "hot spots" alanine scanning, and site saturation mutagenesis. Mutations in the PSPG-like motif region and the C2 loop region are more likely to expand donor preference; mutations of the flexible N3 loop region located at the mouth of the substrate-binding cavity produce novel epothilone oligosaccharides. These "hot spots" also functioned in homologues of BsGT-1. The glycosides showed significantly enhanced water solubility and decreased cytotoxicity, although the glycosyl appendages of epothilone B also reduced drug permeability and attenuated antitumor efficacy. This study laid a foundation for the rational engineering of other GTs to synthesize valuable small molecules.
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